Linked Life Data

410442

Source:http://linkedlifedata.com/resource/pubmed/id/410442

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1977-12-29
pubmed:abstractText
Gabaculine (5-amino-1,3-cyclohexadienylcarboxylic acid), a naturally occurring amino acid isolated from Streptomyces toyacaenis, is an irreversible inhibitor of bacterial pyridoxal phosphate linked gamma-aminobutyric acid-alpha-ketoglutaric acid transaminase with a t 1/2 (25 degrees C) of 9 min at 3 X 10(-7) M. Gabaculine is a substrate for gamma-aminobutyric acid transaminase. The measured KI is 2.86 X 10(-6) M, and the kcat for its turnover is 1.15 X 10(-2) S-1 at 25 degrees C. When gabaculine is transaminated by the enzyme, it is converted to a cyclohexatrienyl system with one exo double bond. Upon spontaneous aromatization, this high energy intermediate is transformed into a stable m-anthranilic acid derivative (m-carboxyphenylpyridoxamine phosphate), which results in the covalent and irreversible modification of the cofactor. This adduct is bound tightly to the active site of the enzyme and can be liberated under denaturing conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4604-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Mechanism of the irreversible inhibition of gamma-aminobutyric acid-alpha-ketoglutaric acid transaminase by the neutrotoxin gabaculine.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.